KGP1_BOVIN
ID KGP1_BOVIN Reviewed; 671 AA.
AC P00516; P21136;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=cGMP-dependent protein kinase 1;
DE Short=cGK 1;
DE Short=cGK1;
DE EC=2.7.11.12;
DE AltName: Full=cGMP-dependent protein kinase I;
DE Short=cGKI;
GN Name=PRKG1; Synonyms=PRKG1B, PRKGR1A, PRKGR1B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX PubMed=2546820; DOI=10.1016/0014-5793(89)81453-x;
RA Wernet W., Flockerzi V., Hofmann F.;
RT "The cDNA of the two isoforms of bovine cGMP-dependent protein kinase.";
RL FEBS Lett. 251:191-196(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC TISSUE=Testis;
RX PubMed=9099696; DOI=10.1074/jbc.272.16.10522;
RA Ruth P., Pfeifer A., Kamm S., Klatt P., Dostmann W.R., Hofmann F.;
RT "Identification of the amino acid sequences responsible for high affinity
RT activation of cGMP kinase Ialpha.";
RL J. Biol. Chem. 272:10522-10528(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-18; 90-375 AND 408-671, AND ACETYLATION AT SER-2.
RX PubMed=6091741; DOI=10.1021/bi00313a030;
RA Takio K., Wade R.D., Smith S.B., Krebs E.G., Walsh K.A., Titani K.;
RT "Guanosine cyclic 3',5'-phosphate dependent protein kinase, a chimeric
RT protein homologous with two separate protein families.";
RL Biochemistry 23:4207-4218(1984).
RN [4]
RP PROTEIN SEQUENCE OF 14-105 (ISOFORM ALPHA), PHOSPHORYLATION AT THR-59, AND
RP BLOCKAGE OF N-TERMINUS.
RC TISSUE=Lung;
RX PubMed=6304091; DOI=10.1016/s0021-9258(20)81923-1;
RA Takio K., Smith S.B., Walsh K.A., Krebs E.G., Titani K.;
RT "Amino acid sequence around a 'hinge' region and its 'autophosphorylation'
RT site in bovine lung cGMP-dependent protein kinase.";
RL J. Biol. Chem. 258:5531-5536(1983).
RN [5]
RP PROTEIN SEQUENCE OF 63-75 (ISOFORM BETA).
RC TISSUE=Aorta;
RX PubMed=2537306; DOI=10.1016/s0021-9258(19)84976-1;
RA Wolfe L., Francis S.H., Corbin J.D.;
RT "Properties of a cGMP-dependent monomeric protein kinase from bovine
RT aorta.";
RL J. Biol. Chem. 264:4157-4162(1989).
RN [6]
RP PROTEIN SEQUENCE OF 374-410, AND ATP-BINDING AT LYS-390.
RX PubMed=6274862; DOI=10.1016/s0021-9258(19)68256-6;
RA Hashimoto E., Takio K., Krebs E.G.;
RT "Amino acid sequence at the ATP-binding site of cGMP-dependent protein
RT kinase.";
RL J. Biol. Chem. 257:727-733(1982).
RN [7]
RP PROTEIN SEQUENCE OF 79-82 (ISOFORM ALPHA), AND CHARACTERIZATION.
RX PubMed=2822399; DOI=10.1111/j.1432-1033.1987.tb13395.x;
RA Heil W.G., Landgraf W., Hofmann F.;
RT "A catalytically active fragment of cGMP-dependent protein kinase.
RT Occupation of its cGMP-binding sites does not affect its phosphotransferase
RT activity.";
RL Eur. J. Biochem. 168:117-121(1987).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=1325910; DOI=10.1111/j.1432-1033.1992.tb17209.x;
RA Keilbach A., Ruth P., Hofmann F.;
RT "Detection of cGMP dependent protein kinase isozymes by specific
RT antibodies.";
RL Eur. J. Biochem. 208:467-473(1992).
RN [9]
RP INTERACTION WITH IRAG1.
RX PubMed=10724174; DOI=10.1038/35004606;
RA Schlossmann J., Ammendola A., Ashman K., Zong X., Huber A., Neubauer G.,
RA Wang G.-X., Allescher H.-D., Korth M., Wilm M., Hofmann F., Ruth P.;
RT "Regulation of intracellular calcium by a signalling complex of IRAG, IP3
RT receptor and cGMP kinase Ibeta.";
RL Nature 404:197-201(2000).
RN [10]
RP INTERACTION WITH IRAG1.
RX PubMed=11309393; DOI=10.1074/jbc.m101530200;
RA Ammendola A., Geiselhoeringer A., Hofmann F., Schlossmann J.;
RT "Molecular determinants of the interaction between the inositol 1,4,5-
RT trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP
RT kinase Ibeta.";
RL J. Biol. Chem. 276:24153-24159(2001).
RN [11]
RP SUBUNIT.
RX PubMed=12480535; DOI=10.1016/s0006-291x(02)02799-7;
RA Koller A., Schlossmann J., Ashman K., Uttenweiler-Joseph S., Ruth P.,
RA Hofmann F.;
RT "Association of phospholamban with a cGMP kinase signaling complex.";
RL Biochem. Biophys. Res. Commun. 300:155-160(2003).
RN [12]
RP INTERACTION WITH IRAG1.
RX PubMed=16166082; DOI=10.1074/jbc.m507021200;
RA Casteel D.E., Boss G.R., Pilz R.B.;
RT "Identification of the interface between cGMP-dependent protein kinase
RT Ibeta and its interaction partners TFII-I and IRAG reveals a common
RT interaction motif.";
RL J. Biol. Chem. 280:38211-38218(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 79-356 IN COMPLEX WITH CAMP.
RX PubMed=21893290; DOI=10.1016/j.str.2011.06.012;
RA Osborne B.W., Wu J., McFarland C.J., Nickl C.K., Sankaran B., Casteel D.E.,
RA Woods V.L. Jr., Kornev A.P., Taylor S.S., Dostmann W.R.;
RT "Crystal structure of cGMP-dependent protein kinase reveals novel site of
RT interchain communication.";
RL Structure 19:1317-1327(2011).
CC -!- FUNCTION: Serine/threonine protein kinase that acts as key mediator of
CC the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates
CC PRKG1, which phosphorylates serines and threonines on many cellular
CC proteins. Numerous protein targets for PRKG1 phosphorylation are
CC implicated in modulating cellular calcium, but the contribution of each
CC of these targets may vary substantially among cell types. Proteins that
CC are phosphorylated by PRKG1 regulate platelet activation and adhesion,
CC smooth muscle contraction, cardiac function, gene expression, feedback
CC of the NO-signaling pathway, and other processes involved in several
CC aspects of the CNS like axon guidance, hippocampal and cerebellar
CC learning, circadian rhythm and nociception. Smooth muscle relaxation is
CC mediated through lowering of intracellular free calcium, by
CC desensitization of contractile proteins to calcium, and by decrease in
CC the contractile state of smooth muscle or in platelet activation.
CC Regulates intracellular calcium levels via several pathways:
CC phosphorylates IRAG1 and inhibits IP3-induced Ca(2+) release from
CC intracellular stores, phosphorylation of KCNMA1 (BKCa) channels
CC decreases intracellular Ca(2+) levels, which leads to increased opening
CC of this channel. PRKG1 phosphorylates the canonical transient receptor
CC potential channel (TRPC) family which inactivates the associated inward
CC calcium current. Another mode of action of NO/cGMP/PKGI signaling
CC involves PKGI-mediated inactivation of the Ras homolog gene family
CC member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of
CC this protein in myriad processes: regulation of RHOA translocation;
CC decreasing contraction; controlling vesicle trafficking, reduction of
CC myosin light chain phosphorylation resulting in vasorelaxation.
CC Activation of PRKG1 by NO signaling alters also gene expression in a
CC number of tissues. In smooth muscle cells, increased cGMP and PRKG1
CC activity influence expression of smooth muscle-specific contractile
CC proteins, levels of proteins in the NO/cGMP signaling pathway, down-
CC regulation of the matrix proteins osteopontin and thrombospondin-1 to
CC limit smooth muscle cell migration and phenotype. Regulates
CC vasodilator-stimulated phosphoprotein (VASP) functions in platelets and
CC smooth muscle (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.12;
CC -!- ACTIVITY REGULATION: In the absence of cGMP, PRKG1 activity is
CC suppressed by autoinhibitory contacts. {ECO:0000250}.
CC -!- SUBUNIT: Isoform alpha: parallel homodimer or heterodimer and also
CC heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of
CC dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets
CC PRKG1 to stress fibers to mediate smooth muscle cell relaxation and
CC vasodilation in responses to rises in cGMP (By similarity). Isoform
CC beta: antiparallel homodimer. Part of cGMP kinase signaling complex at
CC least composed of ACTA2/alpha-actin, CNN1/calponin H1,
CC PLN/phospholamban, PRKG1 and ITPR1. Interacts with IRAG1 (By
CC similarity). Forms a stable complex with ITPR1, IRAG1, and isoform beta
CC of PRKG1 (By similarity). Interacts with TRPC7 (via ankyrin repeat
CC domain) (By similarity). Isoform alpha interacts with RGS2 (By
CC similarity). Interacts with GTF2I (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P00516-1; P00516-1: PRKG1; NbExp=2; IntAct=EBI-10094497, EBI-10094497;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with
CC TRPC7 in the plasma membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha; Synonyms=CGK1-alpha;
CC IsoId=P00516-1; Sequence=Displayed;
CC Name=Beta; Synonyms=CGK1-beta;
CC IsoId=P00516-2, P21136-1;
CC Sequence=VSP_038713;
CC -!- TISSUE SPECIFICITY: High concentrations are detected in various smooth
CC muscle: lung, rumen, trachea, aorta, uterus and stomach. Isoform alpha
CC is expressed predominantly in heart, cerebellum and lung, whereas the
CC beta isoform is expressed in high concentrations in trachea, aorta,
CC stomach and uterus. {ECO:0000269|PubMed:1325910}.
CC -!- DOMAIN: Composed of an N-terminal leucine-zipper domain followed by an
CC autoinhibitory domain, which mediate homodimer formation and inhibit
CC kinase activity, respectively. Next, two cGMP-binding domains are
CC followed by the catalytic domain at the C-terminus. Binding of cGMP to
CC cGMP-binding domains results in a conformational change that activates
CC kinase activity by removing the autoinhibitory domain from the
CC catalytic cleft leaving the catalytic domain free to phosphorylate
CC downstream substrates. Isoforms alpha and beta have identical cGMP-
CC binding and catalytic domains but differ in their leucine zipper and
CC autoinhibitory sequences and therefore differ in their dimerization
CC substrates and kinase enzyme activity.
CC -!- DOMAIN: Heterotetramerization is mediated by the interaction between a
CC coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS,
CC the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.
CC -!- PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.
CC -!- PTM: 65 kDa monomer is produced by proteolytic cleavage.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000305}.
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DR EMBL; X16086; CAA34214.1; -; mRNA.
DR EMBL; X54289; CAA38184.1; -; mRNA.
DR EMBL; Y08961; CAA70155.1; -; mRNA.
DR PIR; A00619; OKBOG.
DR PIR; S05035; S05035.
DR RefSeq; NP_776861.1; NM_174436.2. [P00516-1]
DR RefSeq; XP_005225410.1; XM_005225353.2. [P00516-2]
DR PDB; 3SHR; X-ray; 2.50 A; A/B=79-356.
DR PDBsum; 3SHR; -.
DR AlphaFoldDB; P00516; -.
DR BMRB; P00516; -.
DR SASBDB; P00516; -.
DR SMR; P00516; -.
DR BioGRID; 159293; 2.
DR CORUM; P00516; -.
DR DIP; DIP-59143N; -.
DR IntAct; P00516; 3.
DR STRING; 9913.ENSBTAP00000030518; -.
DR BindingDB; P00516; -.
DR ChEMBL; CHEMBL3183; -.
DR iPTMnet; P00516; -.
DR PRIDE; P00516; -.
DR Ensembl; ENSBTAT00000024490; ENSBTAP00000024490; ENSBTAG00000018404. [P00516-1]
DR Ensembl; ENSBTAT00000030539; ENSBTAP00000030518; ENSBTAG00000018404. [P00516-2]
DR GeneID; 282004; -.
DR KEGG; bta:282004; -.
DR CTD; 5592; -.
DR VEuPathDB; HostDB:ENSBTAG00000018404; -.
DR eggNOG; KOG0614; Eukaryota.
DR GeneTree; ENSGT00940000154704; -.
DR InParanoid; P00516; -.
DR OMA; XTHYENG; -.
DR BRENDA; 2.7.11.12; 908.
DR Reactome; R-BTA-392517; Rap1 signalling.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000018404; Expressed in oocyte and 90 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR002374; cGMP_dep_kinase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031831; PKcGMP_CC.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF16808; PKcGMP_CC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR PRINTS; PR00104; CGMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW ATP-binding; cGMP; cGMP-binding; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6091741"
FT CHAIN 2..671
FT /note="cGMP-dependent protein kinase 1"
FT /id="PRO_0000086114"
FT DOMAIN 360..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 620..671
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 2..102
FT /note="Required for dimerization"
FT REGION 9..44
FT /note="Leucine-zipper"
FT REGION 50..75
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 103..220
FT /note="cGMP-binding, high affinity"
FT /evidence="ECO:0000250"
FT REGION 221..341
FT /note="cGMP-binding, low affinity"
FT /evidence="ECO:0000250"
FT REGION 635..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..59
FT /evidence="ECO:0000250"
FT COMPBIAS 651..671
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 167..170
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:21893290,
FT ECO:0007744|PDB:3SHR"
FT BINDING 167..170
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 177..178
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:21893290,
FT ECO:0007744|PDB:3SHR"
FT BINDING 177..178
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 282
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 291..294
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 301..302
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 336
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 366..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 78..79
FT /note="Cleavage"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6091741"
FT MOD_RES 59
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:6304091"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0C605"
FT DISULFID 43
FT /note="Interchain"
FT VAR_SEQ 1..89
FT /note="MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPST
FT HIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSER -> MGTLRDLQYALQEKIEEL
FT RQRDALIDELELELDQKDELIQKLQNELDKYRSVIRPATQQAQKQSASTLQGEPRTKRQ
FT AISAEPTAFDIQDLSHVTLPFYPKSPQ (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:2546820,
FT ECO:0000303|PubMed:9099696"
FT /id="VSP_038713"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:3SHR"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3SHR"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 194..216
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:3SHR"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 257..270
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3SHR"
FT STRAND 302..317
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:3SHR"
FT HELIX 333..354
FT /evidence="ECO:0007829|PDB:3SHR"
SQ SEQUENCE 671 AA; 76419 MW; 9FE7A48422DA9CDF CRC64;
MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR
AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY
PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT
VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET
HYENGEYIIR QGARGDTFFI ISKGKVNVTR EDSPNEDPVF LRTLGKGDWF GEKALQGEDV
RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF
NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF
IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI
IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD
YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS
ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDNDEPP
PDDNSGWDID F
